The proposed research seeks to elucidate chemical, ultrastructural and metabolic characteristics of the title subject. Periplasmic-bodies (P.B), i.e. vesicles arising from the protoplasmic membrane, are postulated to be involved in the translocation of glycoprotein enzymes destined for the periplasmic space. Analogous structures arise in the periplasmic space of pathogenic yeasts after sub-lethal doses of polyenes (e.g. Amphotericin B), and these vesicles are postulated to be the yeast's device for excluding segments of denatured membrane. A non-pathogen, Saccharomyces rouxii, has a propensity for forming long-lived P.B., and is proposed as a model for developing separation methods for P.B. This methodology would then be applied to a pathogenic yeast, Histoplasma capsulatum, treated with fungistatic levels of Amp. B to see if P.B. membranes are enriched in Amp. B. The cell envelope is the yeast cell's interface with the environment and mediates the signals for endogenous trehalose and glycogen turnover. This program will concentrate on the enzymes of degradation, i.e. trehalase and phosphorylase, their activation by a cyclic 3',5' -adenosine monophosphate (C-AMP) mediated system, and their inhibition by thioanalogs such as 5-thioglucose and thiothrehalose. That work will involve Candida albicans and Torulopsis glabrata. Cytochemical localization of key enzymes beta-fructofuranosidase, trehalase, adenyl cyclase, and phosphodiesterase, and also specific staining for glycogen will complement the biochemical research. C-AMP enzymology and cytochemistry will also be explored in connection with dimorphism in H. capsulatum, C. albicans, and Blastomyces dermatitidis. Current therapy for systemic fungal infections involves nephrotoxic compounds. A long range goal of this research is to propose methods for inhibiting fungal cell growth in the compromised host.